Peter Shier has written: 'Characterization of the gene encoding the insulin receptor-related receptor, IRR : a putative receptor for a member of the insulin family'
tyrosine kinase receptor!!
INSR is the acronym for Insulin Receptor. The insulin receptor watches over the action of insulin. INSR also stands for Insert, Input Shift Register and Integrated Nucleus of Sphygmomanometry Research.
are located in the same areas of the hypothalamus.
Insulin does crosses the blood brain barrier. Insulin crosses the blood brain barrier through the process of receptor-mediated transcytosis.
The membrane proteins that attach to specific hormones such as insulin are called receptor proteins.
Like the receptors for other protein hormones, the receptor for insulin is embedded in the plasma membrane. The insulin receptor is composed of two alpha subunits and two beta subunits linked by disulfide bonds. The alpha chains are entirely extracellular and house insulin binding domains, while the linked beta chains penetrate through the plasma membrane. The insulin receptor is a tyrosine kinase. In other words, it functions as an enzyme that transfers phosphate groups from ATP to tyrosine residues on intracellular target proteins. Binding of insulin to the alpha subunits causes the beta subunits to phosphorylate themselves (autophosphorylation), thus activating the catalytic activity of the receptor. The activated receptor then phosphorylates a number of intracellular proteins, which in turn alters their activity, thereby generating a biological response. Several intracellular proteins have been identified as phosphorylation substrates for the insulin receptor, the best-studied of which is insulin receptor substrate 1 or IRS-1. When IRS-1 is activated by phosphorylation, a lot of things happen. Among other things, IRS-1 serves as a type of docking center for recruitment and activation of other enzymes that ultimately mediate insulin's effects. from yo mama
Bradley Allan Petrisor has written: 'Analysis of the insulin receptor-related gene promoter'
1. Insulin binding to insulin receptor tyrosine kinase on hepatocyte: increased glucose uptake, increased glycogen and fatty acid production and decreased catabolism in general (decreased gluconeogenesis, lipolysis, and proteolysis). Insulin binding causes receptor dimerization and self-phosphorylation. Phosphorylated receptor recruits scaffold proteins and downstream target proteins and phosphorylate them. Phosphorylated target proteins serve as kinases and activate or deactivate other proteins by phosphorylation, effecting appropriate effects. 2. Erythropoietin binding to EPO cytokine receptor on Common Myeloid Progenitor cell: eventual differentiation into erythrocyte. Cytokine receptor induces the Jak/STAT pathway resulting in altered gene expression by transcription factors, drastically changing the function and morphology of the cell.
It's shape is specific for every specific molecule.
This is a typical muscle cell, you the insulin receptor at the top of page within the membrane of the cell. That insulin receptor sends a signal over to the Glut 4 glucose channel in the membrane to the left of the insulin receptor in which sugers enter the cell. The insulin hormone also sends many signals all over the inside of the cells cytoplasm, and into the nucleus on the bottom of page where transcription of genes takes place. In this case a growth hormone is made from a gene, and that growth hormone regulates the insulin and thereby the uptake of glucose into the cell. A type of negative feedback inhibition loop system, so the cell doesn't get too much intake of suger. That growth hormone controls this from happening. David Hagert Researcher medical
There are several different types of hormones and receptors that meet. The types are peptide hormone receptor, lipid-soluable hormone receptor, thyroid stimulating hormone, insulin hormone, leutinizing hormone, and many more.